Multiple Wavelength Anomalous Diffraction (MAD) Crystal Structure of Rusticyanin: a Highly Oxidizing Cupredoxin with Extreme Acid Stability

Walter, R.L.; Ealick, S.E.; Friedman, Alan M.; Blake, Robert C.; Proctor, Peter; Shoham, Menachem

doi:10.1006/jmbi.1996.0612

Cited by 124 publications

(102 citation statements)

References 59 publications

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“…The latter value compares favorably with those of 330 mg/ml for hemoglobin in red blood cells (42) and 300 -400 mg/ml for macromolecules in the interior of Escherichia coli (43). The volume of a single rusticyanin molecule is ϳ20 nm 3 , as determined using either the value of 0.73 cm 3 /g for the average partial specific volume of a globular protein (44) or the actual dimensions of the purified rusticyanin obtained from structural studies by x-ray crystallographic (45) or multidimensional NMR means (46). Consequently, the rusticyanin protein at 350 mg/ml occupies 4.6 ϫ 10 16 nm 3 or 21% of the total volume in the periplasmic space.…”

Section: Discussionmentioning

confidence: 88%

The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant

Painter

Ban

et al. 2015

Journal of Biological Chemistry

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Background:The order of electron transfer in the respiratory chain of Acidithiobacillus ferrooxidans is unknown. Results:The multicenter respiratory chain functioned as an ensemble with a single macroscopic rate constant. Conclusion:The crowded respiratory proteins behaved as would a single protein with a common standard reduction potential of 650 mV. Significance: In situ spectroscopy constitutes a new and effective means to study cellular respiration.

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Section: Discussionmentioning

confidence: 88%

The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant

Painter

Ban

et al. 2015

Journal of Biological Chemistry

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“…a blueshift of the charge transfer band from 597 to 577 nm (11). Apart from the blueshift, the charge transfer band was seen to persist up to pH values of about 10, demonstrating that the overall distorted tetrahedral ligand geometry (involving one cysteine-, one methionine, and two histidine residues (24,25), see Fig. 6) was maintained up to this pH value.…”

Section: Rcy In the Complex With Cytochrome C 4 Resembles Free Rcy Atmentioning

confidence: 84%

“…Rusticyanin, by contrast, is an acid-stable protein and the pK value of the N ␦ protonation site therefore needs to be shifted to pH values significantly below pH 2 in order to assure integrity of the copper site at the physiological pH values of the organism (24,25). Consequently, the above described pK value on the reduced form of the protein was not observed in RCy (26).…”

Section: Role Of the Unique Redox Complex In Electron Transport Of Thmentioning

confidence: 99%

Interaction-induced Redox Switch in the Electron Transfer Complex Rusticyanin-Cytochrome c 4

Giudici‐Orticoni

Guerlesquin

Bruschi

et al. 1999

Journal of Biological Chemistry

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The blue copper protein rusticyanin isolated from the acidophilic proteobacterium Thiobacillus ferrooxidans displays a pH-dependent redox midpoint potential with a pK value of 7 on the oxidized form of the protein. The nature of the alterations of optical and EPR spectra observed above the pK value indicated that the redoxlinked deprotonation occurs on the ⑀-nitrogen of the histidine ligands to the copper ion. Complex formation between rusticyanin and its probable electron transfer partner, cytochrome c 4 , induced a decrease of rusticyanin's redox midpoint potential by more than 100 mV together with spectral changes similar to those observed above the pK value of the free form. Complex formation thus substantially modifies the pK value of the surface-exposed histidine ligand to the copper ion and thereby tunes the redox midpoint potential of the copper site. Comparisons with reports on other blue copper proteins suggest that the surface-exposed histidine ligand is employed as a redox tuning device by many members of this group of soluble electron carriers.

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“…We also investigated 4AZU (1.90 Å) 31 for Az, to address the possible effects of species differences on the NMR hyperfine shift predictions. For Rc, 1RCY 32 (1.90 Å) was also used to investigate an alternative hydrogen-bonding pattern involving the His ligand, as compared to that seen in the 2CAK structure. In each of the protein X-ray structures used in the calculations, hydrogen positions were set to standard values: R CH = 1.09 Å and R NH = 1.01 Å.…”

Section: Computational Detailsmentioning

confidence: 99%

NMR Hyperfine Shifts in Blue Copper Proteins: A Quantum Chemical Investigation

Zhang

Oldfield

2008

J. Am. Chem. Soc.

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We present the results of the first quantum chemical investigations of 1 H NMR hyperfine shifts in the blue copper proteins (BCPs): amicyanin, azurin, pseudoazurin, plastocyanin, stellacyanin, and rusticyanin. We find that very large structural models that incorporate extensive hydrogen bond networks, as well as geometry optimization, are required to reproduce the experimental NMR hyperfine shift results, the best theory vs experiment predictions having R 2 = 0.94, a slope = 1.01, and a SD = 40.5 ppm (or ~4.7% of the overall ~860 ppm shift range). We also find interesting correlations between the hyperfine shifts and the bond and ring critical point properties computed using atoms-in-molecules theory, in addition to finding that hyperfine shifts can be well-predicted by using an empirical model, based on the geometry-optimized structures, which in the future should be of use in structure refinement.

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Multiple Wavelength Anomalous Diffraction (MAD) Crystal Structure of Rusticyanin: a Highly Oxidizing Cupredoxin with Extreme Acid Stability

Cited by 124 publications

References 59 publications

The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant

The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant

Interaction-induced Redox Switch in the Electron Transfer Complex Rusticyanin-Cytochrome c 4

NMR Hyperfine Shifts in Blue Copper Proteins: A Quantum Chemical Investigation

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